Universität Bielefeld, Fakultät für Physik, Bielefeld, Germany.
Biophys J. 2012 Mar 7;102(5):1184-93. doi: 10.1016/j.bpj.2012.01.037. Epub 2012 Mar 6.
In dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasing force until the chemical bond breaks. Repeating the same experiment many times results in a broad distribution of rupture forces, whose quantitative interpretation represents a formidable theoretical challenge. In this study we address the situation that more than a single molecular bond is involved in one experimental run, giving rise to multiple rupture events that are even more difficult to analyze and thus are usually eliminated as far as possible from the further evaluation of the experimental data. We develop and numerically solve a detailed model of a complete dynamic force spectroscopy experiment including a possible clustering of molecules on the substrate surface, the formation of bonds, their dissociation under load, and the postprocessing of the force extension curves. We show that the data, remaining after elimination of obvious multiple rupture events, may still contain a considerable number of hidden multiple bonds, which are experimentally indistinguishable from true single bonds, but which have considerable effects on the resulting rupture force statistics and its consistent theoretical interpretation.
在动态力谱学中，（生物）分子复合物会受到逐渐增大的力的作用，直到化学键断裂。多次重复相同的实验会导致断裂力的广泛分布，其定量解释是一个具有挑战性的理论问题。在这项研究中，我们研究了一种情况，即在一次实验运行中涉及多个分子键，导致多个断裂事件，这些事件更难以分析，因此通常尽可能从实验数据的进一步评估中排除。我们开发并数值求解了一个完整的动态力谱学实验的详细模型，包括分子在基底表面的可能聚集、键的形成、在负载下的解离，以及力-延伸曲线的后处理。我们表明，在消除明显的多次断裂事件后，数据中仍可能包含相当数量的隐藏的多重键，这些键与真实的单键在实验上无法区分，但对最终的断裂力统计及其一致的理论解释有很大影响。
